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pH Dependence of the kinetic parameters of nitrotyrosyl-asparaginase

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The kinetic parameters, KM and kcat of the hydrolysis of L-asparagine by nitrotyrosyl-asparaginase have been determined over a wide pH range of 4.50–8.85. It has been shown that the modification of the asparaginase leads to a marked increase in the Michaelis constant and to an insignificant change in kcat. A hypothesis has been put forward concerning the possible participation of the hydroxy group of the tyrosine residue in the formation of the enzyme-substrate complex.

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Additional information

Institute of Organic Synthesis, Academy of Sciences of the Latvian SSR, Riga. Translated from Khimiya Prirodnykh Soedinenii, No. 3, pp. 364–367, May–June, 1978.

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Milman, I.A., Geiman, I.I., Pinka, U.A. et al. pH Dependence of the kinetic parameters of nitrotyrosyl-asparaginase. Chem Nat Compd 14, 302–304 (1978). https://doi.org/10.1007/BF00713321

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  • Tyrosine
  • Organic Chemistry
  • Kinetic Parameter
  • Hydroxy Group
  • Tyrosine Residue